PYRR_MYCUA
ID PYRR_MYCUA Reviewed; 187 AA.
AC A0PPI7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Bifunctional protein PyrR {ECO:0000255|HAMAP-Rule:MF_01219};
DE Includes:
DE RecName: Full=Pyrimidine operon regulatory protein {ECO:0000255|HAMAP-Rule:MF_01219};
DE Includes:
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01219};
DE Short=UPRTase {ECO:0000255|HAMAP-Rule:MF_01219};
DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01219};
GN Name=pyrR {ECO:0000255|HAMAP-Rule:MF_01219}; OrderedLocusNames=MUL_1779;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- FUNCTION: Regulates the transcription of the pyrimidine nucleotide
CC (pyr) operon in response to exogenous pyrimidines. {ECO:0000255|HAMAP-
CC Rule:MF_01219}.
CC -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC activity which is not physiologically significant. {ECO:0000255|HAMAP-
CC Rule:MF_01219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01219};
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrR subfamily. {ECO:0000255|HAMAP-Rule:MF_01219}.
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DR EMBL; CP000325; ABL04256.1; -; Genomic_DNA.
DR RefSeq; WP_011739876.1; NC_008611.1.
DR AlphaFoldDB; A0PPI7; -.
DR SMR; A0PPI7; -.
DR STRING; 362242.MUL_1779; -.
DR EnsemblBacteria; ABL04256; ABL04256; MUL_1779.
DR KEGG; mul:MUL_1779; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_0_0_11; -.
DR OMA; PIQPDFC; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01219; PyrR; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR023050; PyrR.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..187
FT /note="Bifunctional protein PyrR"
FT /id="PRO_1000053851"
FT MOTIF 109..121
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ SEQUENCE 187 AA; 20071 MW; 596C0A88D6C2EFDD CRC64;
MGAANDAVDG RELMSAAVVG RTISRIAHQI IEKTALDSPD SPRVVLLGIP TRGVILASRL
AANIGEYSGI EVDHGALDIT LYRDDLMSKP PRPLEETEIP AGGVDDALVI LVDDVLYSGR
SVRSALDALR DVGRPRSVQL AVLVDRGHRE LPVRADYVGK NVPTARSESV HVQFSEHDGH
DGVVISR
